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Crystal structure of human MPS1 (ttk) C604W mutant in complex with cpd-5

Analyse Crystal structure of human MPS1 (ttk) C604W mutant in complex with cpd-5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5O91
Type: protein
Length: 266 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dual specificity protein kinase ttk
EC: 2.7.12.1
UniProt: P33981
Ligands: C5N
Pockets: 2 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dual specificity protein kinase ttk (EC 2.7.12.1)	protein	266	37% helix, 21% strand	P33981

Ligands and binding sites

C5N · ~{N}-(2,6-diethylphenyl)-8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydropyrazolo[4,3-h]quinazoline-3-carboxamide · ligand · chains A
EDO · 1,2-ethanediol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	493	0.70	0.80	46	C5N
2	54	0.33	0.78	17	empty

Compared structures

5O91 · Crystal structure of human Mps1 (TTK) C604W mutant in complex with Cpd-5 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P33981
Elsewhere: RCSB PDB 5O91 · PDBe 5O91 · UniProt P33981

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